Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.1.1.251: methylated-thiol-coenzyme M methyltransferase

This is an abbreviated version!
For detailed information about methylated-thiol-coenzyme M methyltransferase, go to the full flat file.

Reaction

a [methyl-Co(III) methylated-thiol-specific corrinoid protein]
+
CoM
=
methyl-CoM
+
a [Co(I) methylated-thiol-specific corrinoid protein]

Synonyms

480-kDa CoM methylase, CoM methylase, DMS:CoM methyltransferase, methylthiol:coenzyme M methyltransferase, methylthiol:CoM methyltransferase, methyltransferase II, MMPA:CoM methyltransferase, MtsA

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.251 methylated-thiol-coenzyme M methyltransferase

Metals Ions

Metals Ions on EC 2.1.1.251 - methylated-thiol-coenzyme M methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co3+
-
the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive
Cobalt
-
the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive
Zn2+
-
one zinc atom per polypeptide